Isolation and characterization of ornitho‐kininogen

Makoto Kimura, Tatsuya SUEYOSHI, Katsumi TAKADA, Kosaku TANAKA, Takashi MORITA, Sadaaki IWANAGA

研究成果: ジャーナルへの寄稿記事

33 引用 (Scopus)

抄録

Ornitho‐kininogen was purified from chicken blood plasma by a two‐stage method using chromatography on columns of S‐alkylated papain‐Cellulofine and DEAE‐5PW. The yield was 1.7 mg from 44 ml plasma. The isolated preparation gave a single band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS‐PAGE) with or without 2‐mercaptoethanol and on disc/polyacrylamide gel electrophoresis. The relative molecular mass, Mr, of ornitho‐kininogen was estimated as 74000 on SDS‐PAGE using the Ferguson plot method. Ornitho‐kininogen was found to have the similar properties to those of mammalian high‐Mr kininogen, in terms of the amino acid composition, molecular mass, and susceptibility to plasma kallikrein. No kininogen corresponding to mammalian low‐Mr kininogen and rat T‐kininogen could be detected in chicken plasma. In fact, ornitho‐kininogen was degraded rapidly by bovine plasma kallikrein, liberating a kinin. This kinin was isolated from the digest by reversed‐phase HPLC. The primary structure of the isolated kinin was determined as Arg1‐Pro2‐Pro3‐Gly4‐Phe5‐Thr6‐Pro7‐Leu8‐Arg9. The sequence of this peptide, named ornitho‐kinin, was similar to that of bradykinin except for the substitution of Thr6 and Leu8 for Ser6 and Phe8. The isolated ornitho‐kinin induced a contraction of chicken smooth muscle and had a strong hypotensive effect in the chicken. However, it did not contract the isolated rat uterus. It is suggested that this specificity difference is due to the replacement of Phe8 by Leu8. The sequence of residues 1–30 of ornitho‐kininogen exhibited 43% identity with that of bovine kininogen.

元の言語英語
ページ(範囲)493-499
ページ数7
ジャーナルEuropean Journal of Biochemistry
168
発行部数3
DOI
出版物ステータス出版済み - 1 1 1987

Fingerprint

Kininogens
ornitho-kinin
Kinins
Chickens
Electrophoresis
Plasma Kallikrein
Polyacrylamide Gel Electrophoresis
Molecular mass
Plasmas
Sodium Dodecyl Sulfate
Rats
Bradykinin
Chromatography
Uterus
Smooth Muscle
Muscle
Blood
Substitution reactions
High Pressure Liquid Chromatography
Amino Acids

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

Kimura, M., SUEYOSHI, T., TAKADA, K., TANAKA, K., MORITA, T., & IWANAGA, S. (1987). Isolation and characterization of ornitho‐kininogen. European Journal of Biochemistry, 168(3), 493-499. https://doi.org/10.1111/j.1432-1033.1987.tb13444.x

Isolation and characterization of ornitho‐kininogen. / Kimura, Makoto; SUEYOSHI, Tatsuya; TAKADA, Katsumi; TANAKA, Kosaku; MORITA, Takashi; IWANAGA, Sadaaki.

:: European Journal of Biochemistry, 巻 168, 番号 3, 01.01.1987, p. 493-499.

研究成果: ジャーナルへの寄稿記事

Kimura, M, SUEYOSHI, T, TAKADA, K, TANAKA, K, MORITA, T & IWANAGA, S 1987, 'Isolation and characterization of ornitho‐kininogen', European Journal of Biochemistry, 巻. 168, 番号 3, pp. 493-499. https://doi.org/10.1111/j.1432-1033.1987.tb13444.x
Kimura M, SUEYOSHI T, TAKADA K, TANAKA K, MORITA T, IWANAGA S. Isolation and characterization of ornitho‐kininogen. European Journal of Biochemistry. 1987 1 1;168(3):493-499. https://doi.org/10.1111/j.1432-1033.1987.tb13444.x
Kimura, Makoto ; SUEYOSHI, Tatsuya ; TAKADA, Katsumi ; TANAKA, Kosaku ; MORITA, Takashi ; IWANAGA, Sadaaki. / Isolation and characterization of ornitho‐kininogen. :: European Journal of Biochemistry. 1987 ; 巻 168, 番号 3. pp. 493-499.
@article{cd31ed894bfb451997d156177ed52ddc,
title = "Isolation and characterization of ornitho‐kininogen",
abstract = "Ornitho‐kininogen was purified from chicken blood plasma by a two‐stage method using chromatography on columns of S‐alkylated papain‐Cellulofine and DEAE‐5PW. The yield was 1.7 mg from 44 ml plasma. The isolated preparation gave a single band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS‐PAGE) with or without 2‐mercaptoethanol and on disc/polyacrylamide gel electrophoresis. The relative molecular mass, Mr, of ornitho‐kininogen was estimated as 74000 on SDS‐PAGE using the Ferguson plot method. Ornitho‐kininogen was found to have the similar properties to those of mammalian high‐Mr kininogen, in terms of the amino acid composition, molecular mass, and susceptibility to plasma kallikrein. No kininogen corresponding to mammalian low‐Mr kininogen and rat T‐kininogen could be detected in chicken plasma. In fact, ornitho‐kininogen was degraded rapidly by bovine plasma kallikrein, liberating a kinin. This kinin was isolated from the digest by reversed‐phase HPLC. The primary structure of the isolated kinin was determined as Arg1‐Pro2‐Pro3‐Gly4‐Phe5‐Thr6‐Pro7‐Leu8‐Arg9. The sequence of this peptide, named ornitho‐kinin, was similar to that of bradykinin except for the substitution of Thr6 and Leu8 for Ser6 and Phe8. The isolated ornitho‐kinin induced a contraction of chicken smooth muscle and had a strong hypotensive effect in the chicken. However, it did not contract the isolated rat uterus. It is suggested that this specificity difference is due to the replacement of Phe8 by Leu8. The sequence of residues 1–30 of ornitho‐kininogen exhibited 43{\%} identity with that of bovine kininogen.",
author = "Makoto Kimura and Tatsuya SUEYOSHI and Katsumi TAKADA and Kosaku TANAKA and Takashi MORITA and Sadaaki IWANAGA",
year = "1987",
month = "1",
day = "1",
doi = "10.1111/j.1432-1033.1987.tb13444.x",
language = "English",
volume = "168",
pages = "493--499",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "3",

}

TY - JOUR

T1 - Isolation and characterization of ornitho‐kininogen

AU - Kimura, Makoto

AU - SUEYOSHI, Tatsuya

AU - TAKADA, Katsumi

AU - TANAKA, Kosaku

AU - MORITA, Takashi

AU - IWANAGA, Sadaaki

PY - 1987/1/1

Y1 - 1987/1/1

N2 - Ornitho‐kininogen was purified from chicken blood plasma by a two‐stage method using chromatography on columns of S‐alkylated papain‐Cellulofine and DEAE‐5PW. The yield was 1.7 mg from 44 ml plasma. The isolated preparation gave a single band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS‐PAGE) with or without 2‐mercaptoethanol and on disc/polyacrylamide gel electrophoresis. The relative molecular mass, Mr, of ornitho‐kininogen was estimated as 74000 on SDS‐PAGE using the Ferguson plot method. Ornitho‐kininogen was found to have the similar properties to those of mammalian high‐Mr kininogen, in terms of the amino acid composition, molecular mass, and susceptibility to plasma kallikrein. No kininogen corresponding to mammalian low‐Mr kininogen and rat T‐kininogen could be detected in chicken plasma. In fact, ornitho‐kininogen was degraded rapidly by bovine plasma kallikrein, liberating a kinin. This kinin was isolated from the digest by reversed‐phase HPLC. The primary structure of the isolated kinin was determined as Arg1‐Pro2‐Pro3‐Gly4‐Phe5‐Thr6‐Pro7‐Leu8‐Arg9. The sequence of this peptide, named ornitho‐kinin, was similar to that of bradykinin except for the substitution of Thr6 and Leu8 for Ser6 and Phe8. The isolated ornitho‐kinin induced a contraction of chicken smooth muscle and had a strong hypotensive effect in the chicken. However, it did not contract the isolated rat uterus. It is suggested that this specificity difference is due to the replacement of Phe8 by Leu8. The sequence of residues 1–30 of ornitho‐kininogen exhibited 43% identity with that of bovine kininogen.

AB - Ornitho‐kininogen was purified from chicken blood plasma by a two‐stage method using chromatography on columns of S‐alkylated papain‐Cellulofine and DEAE‐5PW. The yield was 1.7 mg from 44 ml plasma. The isolated preparation gave a single band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS‐PAGE) with or without 2‐mercaptoethanol and on disc/polyacrylamide gel electrophoresis. The relative molecular mass, Mr, of ornitho‐kininogen was estimated as 74000 on SDS‐PAGE using the Ferguson plot method. Ornitho‐kininogen was found to have the similar properties to those of mammalian high‐Mr kininogen, in terms of the amino acid composition, molecular mass, and susceptibility to plasma kallikrein. No kininogen corresponding to mammalian low‐Mr kininogen and rat T‐kininogen could be detected in chicken plasma. In fact, ornitho‐kininogen was degraded rapidly by bovine plasma kallikrein, liberating a kinin. This kinin was isolated from the digest by reversed‐phase HPLC. The primary structure of the isolated kinin was determined as Arg1‐Pro2‐Pro3‐Gly4‐Phe5‐Thr6‐Pro7‐Leu8‐Arg9. The sequence of this peptide, named ornitho‐kinin, was similar to that of bradykinin except for the substitution of Thr6 and Leu8 for Ser6 and Phe8. The isolated ornitho‐kinin induced a contraction of chicken smooth muscle and had a strong hypotensive effect in the chicken. However, it did not contract the isolated rat uterus. It is suggested that this specificity difference is due to the replacement of Phe8 by Leu8. The sequence of residues 1–30 of ornitho‐kininogen exhibited 43% identity with that of bovine kininogen.

UR - http://www.scopus.com/inward/record.url?scp=0023642538&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023642538&partnerID=8YFLogxK

U2 - 10.1111/j.1432-1033.1987.tb13444.x

DO - 10.1111/j.1432-1033.1987.tb13444.x

M3 - Article

C2 - 3665932

AN - SCOPUS:0023642538

VL - 168

SP - 493

EP - 499

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 3

ER -